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| L-茶氨酸新型酶法制备及其催化工艺优化 | |
| 引用本文： | 李加友,郭丽芸,焦庆才. L-茶氨酸新型酶法制备及其催化工艺优化[J]. 中国生物工程杂志, 2007, 27(10): 34-38 |
| 作者姓名： | 李加友 郭丽芸 焦庆才 |
| 作者单位： | 嘉兴学院生物与化学工程学院 南京大学医药生物技术国家重点实验室 南京大学医药生物技术国家重点实验室 |
| 摘 要： | L-茶氨酸是茶叶中游离氨基酸的主要组成部分，关于其良好的生理活性已有广泛报道。首次报道了来源于Cunnighamella echinulata 9980的L-氨基酰化酶用于高光学纯度的L-茶氨酸的酶法制备。该酶在pH 6.5，底物N-乙酰-DL-茶氨酸浓度为50 mM，且有40 mM CoCl2时催化效果较好。结果表明，在上述条件下，50℃作用12 h得L-茶氨酸22.5 mM，转化率90%。 |
| 关 键 词： | L-茶氨酸 N-乙酰-DL-茶氨酸 Cunnighamella echinulata L-氨基酰化酶 光学拆分 |
| 收稿时间： | 2007-07-17 |
| 修稿时间： | 2007-08-24 |
A Novel Biocatalyst and its optimized process for Preparing L-theanine |
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| LI Jia-you,GUO Li-yun,JIAO Qing-cai. A Novel Biocatalyst and its optimized process for Preparing L-theanine[J]. China Biotechnology, 2007, 27(10): 34-38 | |
| Authors: | LI Jia-you GUO Li-yun JIAO Qing-cai |
| Affiliation: | 1 College of Biological and Chemical Engineering,Jiaxing University,Jiaxing 314001 ,China;2. State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, China |
| Abstract: | L-theanine (γ-glutamylethylamide) is the main free amino acid component of tea and its favorable physiological effects on mammals have been reported. An enzymatic method for optically pure L-theanine production with a new L-aminoacylases-production fungi Cunnighamella echinulata 9980 was developed. The optimum conditions for enzymatic catalysis were at pH 6.5 with 50 mmol/L N-Acyl-DLtheanine and 40 mmol/L CoCl2. After 12-h incubation at 50℃,22.5 mmol/L L-theanine was obtained, the conversion rate against N-Acyl-L-theanine being 90%. Cunnighamella echinulata and the aminoacylase were applied in preparation of L-theanine. |
| Keywords: | Cunnighamella echinulata L-theanine N-Acyl-DL-Theanine Cunnighamella echinulata L-aminoacylase Optical resolution |
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